ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8PAD0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name 3HAO_XANCP
Primary accession number Q8PAD0
Secondary accession numbers None
Integrated into Swiss-Prot on July 11, 2006
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 37)
Name and origin of the protein
Protein name 3-hydroxyanthranilate 3,4-dioxygenase
Synonyms EC 1.13.11.6
3-hydroxyanthranilic acid dioxygenase
HAD
3-hydroxyanthranilate oxygenase
3-HAO
Gene name
OrderedLocusNames: XCC1555
From
Xanthomonas campestris pv. campestris [TaxID: 340] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE012256; AAM40850.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_636926.1; -.
3D structure databases
ModBase Q8PAD0.
Enzyme and pathway databases
BioCyc XCAM190485:XCC1555-MON; -.
Ontologies
GO
GO:0000334; Molecular function: 3-hydroxyanthranilate 3,4-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0008198; Molecular function: ferrous iron binding (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00825; -; 1.
PBIL [Tree]
InterPro IPR010329; 3hydroanth_dOase.
Graphical view of domain structure.
Pfam PF06052; 3-HAO; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR03037; anthran_nbaC; 1.
ProtoNet Q8PAD0.
Genome annotation databases
GeneID 998201; -.
GenomeReviews AE008922_GR; XCC1555.
KEGG xcc:XCC1555; -.
Phylogenomic databases
HOGENOM Q8PAD0; -.
Genome annotation databases
CMR Q8PAD0; XCC1555.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   176  176     3-hydroxyanthranilate 3,4-dioxygenase. PRO_0000245482
METAL   48    48        Iron 1; catalytic (By similarity). 
METAL   54    54        Iron 1; catalytic (By similarity). 
METAL   92    92        Iron 1; catalytic (By similarity). 
METAL   121   121        Iron 2 (By similarity). 
METAL   124   124        Iron 2 (By similarity). 
METAL   158   158        Iron 2 (By similarity). 
METAL   161   161        Iron 2 (By similarity). 
BINDING   44    44        Dioxygen (By similarity). 
BINDING   54    54        Substrate (By similarity). 
BINDING   96    96        Substrate (By similarity). 
BINDING   106   106        Substrate (By similarity). 
Sequence information
Length: 176 AA [This is the length of the unprocessed precursor] Molecular weight: 20128 Da [This is the MW of the unprocessed precursor] CRC64: 3C2FDD218C8458D4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLVPPINLHA WVEQHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE 

        70         80         90        100        110        120 
GEMVLKVQDD GTARDIPIRA GEIFLLPPKV PHSPQRAAGS IGLVIERERL PHEQDGLQWY 

       130        140        150        160        170 
CPQCNHKLYE AMFPLENIET DFPPVFDHFY RSLALRTCTQ CGHVHPAPER YAAVEA 

Q8PAD0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!